The AJ521 antibody labels the human CD1b protein by immunofluorescence

Maxit, Orlane Laurentine; Ameti, Ilhan; Hussami, Sara; Spedaliero, Sébastien; Manoukian, Arec; Richard, Maxime; Verdon, Margaux Océane; Bulla, Monica; Sassi, Ali; Guilhen, Cyril

doi:10.24450/journals/abrep.2020.e121

Cited by 2 publications

(1 citation statement)

References 4 publications

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“…For immunofluorescence detection we used antibodies recognizing the cytosolic domain of Cisd1(RB251; mouse Fc) [ 11 ], the cytosolic domain of Cisd2 (RB253; mouse Fc) [ 12 ], the extracellular domain of CD1b (AJ521; mouse Fc) [ 22 ], the human giantin (AA341; human Fc) [ 23 ] and the human COPI complex (RB498; rabbit Fc) [ 15 , 16 ]. All antibodies were produced by the Geneva Antibody Facility ( https://www.unige.ch/medecine/antibodies/ ) as scFv-Fc minibodies fused with the indicated Fc portion.…”

Section: Methodsmentioning

confidence: 99%

Intracellular targeting of Cisd2/Miner1 to the endoplasmic reticulum

Bian

Marchetti

Hammel

et al. 2021

BMC Mol and Cell Biol

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Background Cisd1 and Cisd2 proteins share very similar structures with an N-terminal membrane-anchoring domain and a C-terminal cytosolic domain containing an iron-cluster binding domain and ending with a C-terminal KKxx sequence. Despite sharing a similar structure, Cisd1 and Cisd2 are anchored to different compartments: mitochondria for Cisd1 and endoplasmic reticulum for Cisd2. The aim of this study was to identify the protein motifs targeting Cisd2 to the ER and ensuring its retention in this compartment. Results We used new recombinant antibodies to localize Cisd1 and Cisd2 proteins, as well as various protein chimeras. Cisd2 is targeted to the ER by its N-terminal sequence. It is then retained in the ER by the combined action of a C-terminal COPI-binding KKxx ER retrieval motif, and of an ER-targeting transmembrane domain. As previously reported for Cisd1, Cisd2 can alter the morphology of the compartment in which it accumulates. Conclusion Although they share a very similar structure, Cisd1 and Cisd2 use largely different intracellular targeting motifs to reach their target compartment (mitochondria and endoplasmic reticulum, respectively).

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Section: Methodsmentioning

confidence: 99%

Intracellular targeting of Cisd2/Miner1 to the endoplasmic reticulum

Bian

Marchetti

Hammel

et al. 2021

BMC Mol and Cell Biol

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Short transmembrane domains target type II proteins to the Golgi apparatus and type I proteins to the endoplasmic reticulum

Bian,

Marchetti,

Dias

et al. 2024

Journal of Cell Science

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Transmembrane domains (TMDs) contain information targeting membrane proteins to various compartments of the secretory pathway. In previous studies, short or hydrophilic TMDs have been shown to target membrane proteins either to the endoplasmic reticulum (ER), or to the Golgi apparatus. The basis for differential sorting to the ER and to the Golgi apparatus remained however unclear. To clarify this point, we analyzed quantitatively the intracellular targeting of a collection of proteins exhibiting a single TMD. Our results reveal that membrane topology is a major targeting element in the early secretory pathway: type I proteins with a short transmembrane domain are targeted to the ER, and type II proteins to the Golgi apparatus. A combination of three features accounts for the sorting of simple membrane proteins in the secretory pathway: membrane topology, length and hydrophilicity of the TMD, and size of the cytosolic domain. By clarifying the rules governing sorting to the ER and to the Golgi apparatus, our study may revive the search for sorting mechanisms in the early secretory pathway.

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The AJ521 antibody labels the human CD1b protein by immunofluorescence

Abstract: The recombinant antibody AJ521 detects by immunofluorescence the human CD1b surface protein in paraformaldehyde-fixed cells.

Cited by 2 publications

References 4 publications

Intracellular targeting of Cisd2/Miner1 to the endoplasmic reticulum

Intracellular targeting of Cisd2/Miner1 to the endoplasmic reticulum

Short transmembrane domains target type II proteins to the Golgi apparatus and type I proteins to the endoplasmic reticulum

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